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StAR-related lipid transfer domain-containing protein 13 (STARD13) is an enzyme classified as a Rho GTPase-activating protein (RhoGAP) that regulates the Rho family of small GTPases, particularly RhoA and CDC42. The protein features an N-terminal sterile alpha motif (SAM), a RhoGAP domain, and a C-terminal START (StAR-related lipid transfer) domain, mediating protein-protein interactions, GTPase activity, and lipid binding. STARD13 acts primarily as a tumor suppressor, with roles in inhibiting cell proliferation, regulating cell motility, and reorganizing the cytoskeleton. It is involved in the control of focal adhesion dynamics, cell migration, and may suppress tumor initiation and progression in hepatocellular carcinoma, breast cancer, and other malignancies. Expression of STARD13 is frequently lost or reduced in several cancer types, correlating with increased malignancy and poor prognosis. Modulation of STARD13 by microRNAs, altered splicing, or mutation can contribute to tumorigenesis. No small-molecule or biologic drugs directly target STARD13 as of now.
Not applicable for approved drugs, as no drugs presently target STARD13 as a primary pharmacological target. If targeted, hypothetical MOA would include: activation or stabilization of GAP activity to enhance tumor suppression, or modulation of cytoskeletal dynamics to influence cell motility and proliferation.
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